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Home > Protein Information

Gelsolin (GS)

GS is a cytoskeleton protein, which has the effect of improving cell activity and plasticity. Gelsolin, one of the members of the GS superfamily, is an important actin binding protein that controls the structure of actin by cutting off, terminating actin filaments, or aggregating actin into nuclei. In addition to its role in recombinant actin filaments, thrombin plays an important role in cellular activities such as cell movement and control of programmed cell death. In addition, the expression of GS in tumor cells also changed. Mutations in GS are also the basis of some genetic diseases.
Although it was initially considered that thrombin is a tumor suppressor gene, recent studies have found that the expression of thrombin in some tumors is associated with poor prognosis. In vitro, GS has anti-apoptosis and migration functions, and is essential for the invasion of certain types of tumor cells.
By immunohistochemical examination, the researchers found that thrombolysin was highly expressed at the boundary of cancer tissues invading liver organs. Although GS contributes to the formation of patchy pseudofeet during cell migration and the induction of tumor invasion, the exact mechanism is not yet clear. Using overexpression techniques and RNA interference techniques to overexpress or knock out the expression of progestin in colorectal cancer cells, the researchers examined the effect of progestin on invasiveness.
Studies have shown that thrombin is necessary for the invasion of colorectal cancer cells into the basal membrane. Microarray analysis and quantitative PCR studies showed that the overexpression of GS resulted in the up-regulation of invasion genes in tumor cells promoting colorectal cancer, including the matrix degradation of urokinase-type plasminogen activator (uPA).
On the contrary, the expression level of uPA will be reduced and the secretion of uPA will be correspondingly inhibited after the inhibition of GS. The invasion of tumor cells overexpressed with thrombin can be weakened after blocking with specific uPA or its receptor antibody, indicating that uPA/ and its receptor uPAR are crucial for the promotion of tumor cell invasion by thrombin. In conclusion, the study data confirmed that thrombin promoted the invasion of colorectal cancer tumor cells by regulating the uPA/uPAR signaling cascade.
At present, DLDEVELOP co. LTD has developed corresponding GS Elisa products. To get more information, you could contact our professional staff directly or directly to our website:
https://dldevelop.com/Research-reagent/dl-gs-hu.html
https://dldevelop.com/Research-reagent/dl-gs-mu.html

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